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LY66F_HUMAN
ID   LY66F_HUMAN             Reviewed;         297 AA.
AC   Q5SQ64; B0UXB7; O95869; Q7Z5H2; Q96QC7; Q9NZJ1;
DT   26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT   26-FEB-2008, sequence version 2.
DT   03-AUG-2022, entry version 145.
DE   RecName: Full=Lymphocyte antigen 6 complex locus protein G6f;
DE   Flags: Precursor;
GN   Name=LY6G6F; Synonyms=C6orf21, G6F, LY6G6D, NG32;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, INTERACTION WITH GRB2 AND
RP   GRB7, SUBCELLULAR LOCATION, GLYCOSYLATION, PHOSPHORYLATION AT TYR-281, AND
RP   MUTAGENESIS OF TYR-281.
RX   PubMed=12852788; DOI=10.1042/bj20030293;
RA   De Vet E.C.J.M., Aguado B., Campbell R.D.;
RT   "Adaptor signalling proteins Grb2 and Grb7 are recruited by human G6f, a
RT   novel member of the immunoglobulin superfamily encoded in the MHC.";
RL   Biochem. J. 375:207-213(2003).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT SER-39.
RX   PubMed=14656967; DOI=10.1101/gr.1736803;
RA   Xie T., Rowen L., Aguado B., Ahearn M.E., Madan A., Qin S., Campbell R.D.,
RA   Hood L.;
RT   "Analysis of the gene-dense major histocompatibility complex class III
RT   region and its comparison to mouse.";
RL   Genome Res. 13:2621-2636(2003).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Shiina S., Tamiya G., Oka A., Inoko H.;
RT   "Homo sapiens 2,229,817bp genomic DNA of 6p21.3 HLA class I region.";
RL   Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA   Mueller R., Ziegler B.L.;
RT   "Identification of MEGT1, a novel megakaryocyte-specific gene.";
RL   Submitted (OCT-1999) to the EMBL/GenBank/DDBJ databases.
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT THR-107.
RX   PubMed=14574404; DOI=10.1038/nature02055;
RA   Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA   Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA   Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA   Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA   Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA   Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA   Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA   Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA   Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA   French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA   Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA   Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA   Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA   Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA   Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA   Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA   Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA   Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA   Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA   Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA   Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA   Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA   Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA   Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA   Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA   West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA   Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA   Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA   Rogers J., Beck S.;
RT   "The DNA sequence and analysis of human chromosome 6.";
RL   Nature 425:805-811(2003).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA   Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA   Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA   Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA   Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA   Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA   Hunkapiller M.W., Myers E.W., Venter J.C.;
RL   Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN   [7]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [8]
RP   GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-88.
RC   TISSUE=Platelet;
RX   PubMed=16263699; DOI=10.1074/mcp.m500324-mcp200;
RA   Lewandrowski U., Moebius J., Walter U., Sickmann A.;
RT   "Elucidation of N-glycosylation sites on human platelet proteins: a
RT   glycoproteomic approach.";
RL   Mol. Cell. Proteomics 5:226-233(2006).
CC   -!- FUNCTION: May play a role in the downstream signal transduction
CC       pathways involving GRB2 and GRB7. {ECO:0000269|PubMed:12852788}.
CC   -!- SUBUNIT: Homodimer; disulfide-linked. Interacts with GRB2 and GRB7 in a
CC       phosphorylation-dependent manner. {ECO:0000269|PubMed:12852788}.
CC   -!- INTERACTION:
CC       Q5SQ64; P62993: GRB2; NbExp=3; IntAct=EBI-6963742, EBI-401755;
CC       Q5SQ64; Q14451: GRB7; NbExp=2; IntAct=EBI-6963742, EBI-970191;
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:12852788};
CC       Single-pass type I membrane protein {ECO:0000269|PubMed:12852788}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=2;
CC       Name=1;
CC         IsoId=Q5SQ64-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q5SQ64-2; Sequence=VSP_055597;
CC   -!- PTM: N-glycosylated. {ECO:0000269|PubMed:12852788,
CC       ECO:0000269|PubMed:16263699}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAD18078.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC       Sequence=BAB63382.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR   EMBL; AJ496460; CAD42968.1; -; mRNA.
DR   EMBL; AF129756; AAD18078.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BA000025; BAB63382.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; AF195764; AAF35181.1; -; mRNA.
DR   EMBL; AL662899; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL670886; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL805934; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BX248244; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR354443; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR753842; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CR759787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471081; EAX03485.1; -; Genomic_DNA.
DR   EMBL; CH471081; EAX03487.1; -; Genomic_DNA.
DR   EMBL; BC137212; AAI37213.1; -; mRNA.
DR   EMBL; BC137213; AAI37214.1; -; mRNA.
DR   CCDS; CCDS34403.1; -. [Q5SQ64-1]
DR   RefSeq; NP_001003693.1; NM_001003693.1. [Q5SQ64-1]
DR   AlphaFoldDB; Q5SQ64; -.
DR   BioGRID; 129225; 14.
DR   IntAct; Q5SQ64; 2.
DR   MINT; Q5SQ64; -.
DR   STRING; 9606.ENSP00000364992; -.
DR   GlyGen; Q5SQ64; 1 site.
DR   iPTMnet; Q5SQ64; -.
DR   PhosphoSitePlus; Q5SQ64; -.
DR   BioMuta; LY6G6F; -.
DR   DMDM; 172045922; -.
DR   MassIVE; Q5SQ64; -.
DR   PaxDb; Q5SQ64; -.
DR   PeptideAtlas; Q5SQ64; -.
DR   PRIDE; Q5SQ64; -.
DR   ProteomicsDB; 63788; -. [Q5SQ64-1]
DR   ProteomicsDB; 83413; -.
DR   Antibodypedia; 34899; 141 antibodies from 21 providers.
DR   DNASU; 259215; -.
DR   Ensembl; ENST00000375832.5; ENSP00000364992.5; ENSG00000204424.10. [Q5SQ64-1]
DR   Ensembl; ENST00000383420.4; ENSP00000372912.4; ENSG00000243804.1.
DR   Ensembl; ENST00000442105.2; ENSP00000404621.2; ENSG00000241822.3.
DR   Ensembl; ENST00000446062.2; ENSP00000404884.2; ENSG00000239741.3. [Q5SQ64-1]
DR   Ensembl; ENST00000447811.2; ENSP00000409959.2; ENSG00000240008.1. [Q5SQ64-1]
DR   Ensembl; ENST00000453044.2; ENSP00000389102.2; ENSG00000240957.1. [Q5SQ64-1]
DR   Ensembl; ENST00000455632.2; ENSP00000407535.2; ENSG00000243003.3. [Q5SQ64-1]
DR   GeneID; 259215; -.
DR   KEGG; hsa:259215; -.
DR   MANE-Select; ENST00000375832.5; ENSP00000364992.5; NM_001003693.3; NP_001003693.1.
DR   UCSC; uc003nwa.2; human. [Q5SQ64-1]
DR   CTD; 259215; -.
DR   DisGeNET; 259215; -.
DR   GeneCards; LY6G6F; -.
DR   HGNC; HGNC:13933; LY6G6F.
DR   HPA; ENSG00000204424; Tissue enhanced (bone marrow, lymphoid tissue, skin).
DR   MIM; 611404; gene.
DR   neXtProt; NX_Q5SQ64; -.
DR   OpenTargets; ENSG00000204424; -.
DR   OpenTargets; ENSG00000250641; -.
DR   PharmGKB; PA38371; -.
DR   VEuPathDB; HostDB:ENSG00000204424; -.
DR   eggNOG; ENOG502SNF5; Eukaryota.
DR   GeneTree; ENSGT00390000015960; -.
DR   HOGENOM; CLU_071209_0_0_1; -.
DR   InParanoid; Q5SQ64; -.
DR   OMA; PRTICCL; -.
DR   PhylomeDB; Q5SQ64; -.
DR   TreeFam; TF337100; -.
DR   PathwayCommons; Q5SQ64; -.
DR   Reactome; R-HSA-114608; Platelet degranulation.
DR   SignaLink; Q5SQ64; -.
DR   BioGRID-ORCS; 259215; 9 hits in 1046 CRISPR screens.
DR   GenomeRNAi; 259215; -.
DR   Pharos; Q5SQ64; Tbio.
DR   PRO; PR:Q5SQ64; -.
DR   Proteomes; UP000005640; Chromosome 6.
DR   RNAct; Q5SQ64; protein.
DR   Bgee; ENSG00000204424; Expressed in monocyte and 29 other tissues.
DR   ExpressionAtlas; Q5SQ64; baseline and differential.
DR   Genevisible; Q5SQ64; HS.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR   GO; GO:0031092; C:platelet alpha granule membrane; TAS:Reactome.
DR   Gene3D; 2.60.40.10; -; 1.
DR   InterPro; IPR007110; Ig-like_dom.
DR   InterPro; IPR036179; Ig-like_dom_sf.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR003599; Ig_sub.
DR   InterPro; IPR013106; Ig_V-set.
DR   InterPro; IPR026524; LY6G6d/LY6G6f.
DR   PANTHER; PTHR32286; PTHR32286; 1.
DR   Pfam; PF07686; V-set; 1.
DR   SMART; SM00409; IG; 1.
DR   SUPFAM; SSF48726; SSF48726; 1.
DR   PROSITE; PS50835; IG_LIKE; 1.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cell membrane; Disulfide bond; Glycoprotein;
KW   Immunoglobulin domain; Membrane; Phosphoprotein; Reference proteome;
KW   Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..16
FT                   /evidence="ECO:0000255"
FT   CHAIN           17..297
FT                   /note="Lymphocyte antigen 6 complex locus protein G6f"
FT                   /id="PRO_0000318923"
FT   TOPO_DOM        17..235
FT                   /note="Extracellular"
FT                   /evidence="ECO:0000255"
FT   TRANSMEM        236..256
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        257..297
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000255"
FT   DOMAIN          17..122
FT                   /note="Ig-like V-type"
FT   MOD_RES         281
FT                   /note="Phosphotyrosine"
FT                   /evidence="ECO:0000269|PubMed:12852788"
FT   CARBOHYD        88
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000269|PubMed:16263699"
FT   DISULFID        35..106
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT   VAR_SEQ         268..297
FT                   /note="DASIPQFKPEIQVYENIHLARLGPPAHKPR -> GNRMRCYNCGGSPSSSCK
FT                   EAVTTCGEGRPQPGLEQIKLPGNPPVTLIHQHPACVAAHHCNQVETESVGDVTYPAHRD
FT                   CYLGDLCNSAVASHVAPAGILAAAATALTCLLPGLWSG (in isoform 2)"
FT                   /evidence="ECO:0000303|Ref.4"
FT                   /id="VSP_055597"
FT   VARIANT         34
FT                   /note="P -> Q (in dbSNP:rs17200983)"
FT                   /id="VAR_038908"
FT   VARIANT         39
FT                   /note="P -> S (in dbSNP:rs805295)"
FT                   /evidence="ECO:0000269|PubMed:14656967"
FT                   /id="VAR_038909"
FT   VARIANT         107
FT                   /note="A -> T (in dbSNP:rs9267547)"
FT                   /evidence="ECO:0000269|PubMed:14574404"
FT                   /id="VAR_038910"
FT   VARIANT         167
FT                   /note="R -> K (in dbSNP:rs2242653)"
FT                   /id="VAR_038911"
FT   MUTAGEN         281
FT                   /note="Y->F: No phosphorylation. No interaction with GRB2
FT                   and GRB7. No phosphorylation increase of p42/44 MAP
FT                   kinase."
FT                   /evidence="ECO:0000269|PubMed:12852788"
SQ   SEQUENCE   297 AA;  32465 MW;  B4FFB401D70AA308 CRC64;
     MAVLFLLLFL CGTPQAADNM QAIYVALGEA VELPCPSPPT LHGDEHLSWF CSPAAGSFTT
     LVAQVQVGRP APDPGKPGRE SRLRLLGNYS LWLEGSKEED AGRYWCAVLG QHHNYQNWRV
     YDVLVLKGSQ LSARAADGSP CNVLLCSVVP SRRMDSVTWQ EGKGPVRGRV QSFWGSEAAL
     LLVCPGEGLS EPRSRRPRII RCLMTHNKGV SFSLAASIDA SPALCAPSTG WDMPWILMLL
     LTMGQGVVIL ALSIVLWRQR VRGAPGRDAS IPQFKPEIQV YENIHLARLG PPAHKPR
 
 
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